Mutational analysis and a structural model of methyl-directed restriction enzyme Mrr.
The Mrr protein of Escherichia coli K12 is a cryptic Type IV restriction endonuclease whose activity appears to be triggered by high pressure stress. In this report we used high pressure to isolate and analyze several Mrr mutants, and generated a new structural model of the Mrr protein. The activity of a number of spontaneous and strategically constructed Mrr mutants is discussed in the light of this model, providing a first insight into the structure-function relationships of the Mrr enzyme.
Orlowski
Jerzy
J
Laboratory of Bioinformatics and Protein Engineering, International Institute of Molecular and Cell Biology in Warsaw, Ul. Ks. Trojdena 4, 02-109 Warsaw, Poland.
Mebrhatu
Mehari Tesfazgi
MT
Michiels
Chris W
CW
Bujnicki
Janusz M
JM
Aertsen
Abram
A
D000483:Alleles; D000595:Amino Acid Sequence; D004252:DNA Mutational Analysis; D004262:DNA Restriction Enzymes / Q000737:chemistry* / Q000235:genetics*; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011312:Pressure; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship
D029968:Escherichia coli Proteins; D004262:DNA Restriction Enzymes; C070141:Mrr protein, E coli